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acetyl-CoA + AAKKRG
CoA + N-acetyl-AAKKRG
-
-
-
?
acetyl-CoA + ACTH peptide
CoA + ?
-
17 amino acids are identical to the adrenocorticotropin (ACTH) peptide sequence, the ACTH-derived lysines are replaced by arginines to minimize any potential interference by Nalpha-acetylation
-
-
?
acetyl-CoA + actin
?
-
-
-
-
?
acetyl-CoA + an N-terminal-amino acid-[protein]
an N-terminal-Nalpha-acetyl-amino acid-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-valyl-[protein] + CoA
acetyl-CoA + an N-terminal-lysinyl-[androgen receptor]
an N-terminal-Nalpha-acetyl-lysinyl-[androgen receptor] + CoA
-
ARD1 acetylates androgen receptor at lysine 618
-
-
?
acetyl-CoA + an N-terminal-methionyl-[RPM1 protein]
an N-terminal-Nalpha-acetyl-methionyl-[RPM1 protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-methionyl-[SNC1 protein]
an N-terminal-Nalpha-acetyl-methionyl-[SNC1 protein] + CoA
-
NatA specifically acetylates the first met of SNC1 protein
-
-
?
acetyl-CoA + beta-catenin
?
-
-
-
-
?
acetyl-CoA + CAP2
?
-
-
-
-
?
acetyl-CoA + DDDIAAL
CoA + N-acetyl-DDDIAAL
-
-
-
?
acetyl-CoA + DDDIAALRWGRPVGRRRRPVRVYP
CoA + Nalpha-acetyl-DDDIAALRWGRPVGRRRRPVRVYP
-
-
-
?
acetyl-CoA + EEEIAAL
CoA + N-acetyl-EEEIAAL
best substrate
-
-
?
acetyl-CoA + EEEIAALRWGRPVGRRRRPVRVYP
CoA + Nalpha-acetyl-EEEIAALRWGRPVGRRRRPVRVYP
-
-
-
?
acetyl-CoA + GRX3
?
-
-
-
-
?
acetyl-CoA + MEEKVG
CoA + N-acetyl-MEEKVG
-
-
-
?
acetyl-CoA + MLCK
?
-
-
-
-
?
acetyl-CoA + MLGPEGG
CoA + N-acetyl-MLGPEGG
poor substrate
-
-
?
acetyl-CoA + MLGPEGGRWGRPVGRRRRPVRVYP
CoA + Nalpha-acetyl-MLGPEGGRWGRPVGRRRRPVRVYP
-
-
-
?
acetyl-CoA + MSRA
?
-
-
-
-
?
acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
acetyl-CoA + N-terminal L-alanyl-[KVNIK]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[KVNIK]
acetyl-CoA + N-terminal L-alanyl-[RYFRR]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[RYFRR]
acetyl-CoA + N-terminal L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-aspartyl-[DDDIAALRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
acetyl-CoA + N-terminal L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-glutamyl-[EEEIAALRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
acetyl-CoA + N-terminal L-methionyl-[LGPEGGRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-methionyl-[LGPEGGRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-methionyl-[LGPEGGRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-methionyl-[MLGPEGGRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-methionyl-[MMP2]
CoA + H+ + N-terminal Nalpha-acetyl-L-methionyl-[MMP2]
matrix metalloproteinase-2, MMP2, with sequence MEALMAR
-
-
?
acetyl-CoA + N-terminal L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
acetyl-CoA + N-terminal L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[SESSSKSRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-seryl-[KLIEY]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[KLIEY]
acetyl-CoA + N-terminal L-seryl-[RVQIS]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[RVQIS]
acetyl-CoA + NTF2
?
-
-
-
-
?
acetyl-CoA + Orc1p
CoA + Nalpha-acetyl-[Orc1p]
acetyl-CoA + PCNP protein
CoA + Nalpha-acetyl-PCNP protein
-
i.e. PEST proteolytic signal-containing nuclear protein
-
-
?
acetyl-CoA + PDC5
?
-
-
-
-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
acetyl-CoA + peptide
Nalpha-acetylpeptide + CoA
acetyl-CoA + PIL1
?
-
-
-
-
?
acetyl-CoA + POL30
?
-
-
-
-
?
acetyl-CoA + QVATYHRAIKVTVDGPRW
?
-
-
-
-
?
acetyl-CoA + RAD23
?
-
-
-
-
?
acetyl-CoA + RKEQTPVAAKHHVNGNRTVW
?
-
-
-
-
?
acetyl-CoA + RPS12
?
-
-
-
-
?
acetyl-CoA + RUP2
?
-
-
-
-
?
acetyl-CoA + SASEAGVRWGRPVGRRRRP
CoA + Nalpha-acetyl-SASEAGVRWGRPVGRRRRP
-
-
-
?
acetyl-CoA + SESSSKS
CoA + N-acetyl-SESSSKS
-
-
-
?
acetyl-CoA + SESSSKSRWGRPVGRRRRPVRVYP
CoA + Ac-SESSSKSRWGRPVGRRRRPVRVYP
-
high-mobility-group protein A1 sequence
-
-
?
acetyl-CoA + SESSSKSRWGRPVGRRRRPVRVYP
CoA + Nalpha-acetyl-SESSSKSRWGRPVGRRRRPVRVYP
-
-
-
?
acetyl-CoA + silencing facor Sir3p
CoA + Nalpha-acetyl-[silencing factor Sir3p]
acetyl-CoA + SMI1
?
-
-
-
-
?
acetyl-CoA + SNZ2/3
?
-
-
-
-
?
acetyl-CoA + SSGTPT
CoA + N-acetyl-SSGTPT
-
-
-
?
acetyl-CoA + THI20
?
-
-
-
-
?
acetyl-CoA + THI22
?
-
-
-
-
?
acetyl-CoA + THI4
?
-
-
-
-
?
acetyl-CoA + THI6
?
-
-
-
-
?
acetyl-CoA + TIF6
?
-
-
-
-
?
acetyl-CoA + TVHEKKSSRKSEYLLPVAW
?
-
-
-
-
?
acetyl-CoA + VMA6
?
-
-
-
-
?
acetyl-CoA + ZPS1
?
-
-
-
-
?
acetyl-CoA + [histone 2B]
an N-terminal-Nalpha-acetyl-[histone 2B] + CoA
-
-
-
-
?
acetyl-CoA + [iso-1-cytochrome c]
an N-terminal-Nalpha-acetyl-[iso-1-cytochrome c] + CoA
-
-
-
-
?
acetyl-CoA + [Runx2]
[Runx2]-N-terminal-N6-acetyl-L-lysine + CoA
additional information
?
-
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-valyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-valyl-[protein] + CoA
-
-
-
?
acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
-
-
?
acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
-
-
?
acetyl-CoA + N-terminal L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[Arg-Tyr-Phe-Arg-Arg]
-
-
-
?
acetyl-CoA + N-terminal L-alanyl-[KVNIK]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[KVNIK]
DP7 peptide (AKVNIK) is a substrate of NatA and is derived from the protein endoded by groES/Rv3418c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-alanyl-[KVNIK]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[KVNIK]
DP7 peptide (AKVNIK) is a substrate of NatA and is derived from the protein endoded by groES/Rv3418c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-alanyl-[KVNIK]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[KVNIK]
DP7 peptide (AKVNIK) is a substrate of NatA and is derived from the protein endoded by groES/Rv3418c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-alanyl-[RYFRR]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[RYFRR]
DPC peptide (ARYFRR) is a substrate of NatA and is derived from the sequence of S18 RNA protein rpsRS18 of Salmonella typhimurium
-
-
ir
acetyl-CoA + N-terminal L-alanyl-[RYFRR]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[RYFRR]
DPC peptide (ARYFRR) is a substrate of NatA and is derived from the sequence of S18 RNA protein rpsRS18 of Salmonella typhimurium
-
-
ir
acetyl-CoA + N-terminal L-alanyl-[RYFRR]
CoA + H+ + N-terminal Nalpha-acetyl-L-alanyl-[RYFRR]
DPC peptide (ARYFRR) is a substrate of NatA and is derived from the sequence of S18 RNA protein rpsRS18 of Salmonella typhimurium
-
-
ir
acetyl-CoA + N-terminal L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
-
-
-
ir
acetyl-CoA + N-terminal L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-aspartyl-[DDIAALRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
-
-
-
ir
acetyl-CoA + N-terminal L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-glutamyl-[EEIAALRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
-
-
-
?
acetyl-CoA + N-terminal L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[ESSSKSRWGRPVGRRRRPVRVYP]
substrate SESS
-
-
?
acetyl-CoA + N-terminal L-seryl-[KLIEY]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[KLIEY]
DP6 peptide (SKLIEY) is a substrate of NatA and is derived from the protein endoded by tsaE/Rv3422c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-seryl-[KLIEY]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[KLIEY]
DP6 peptide (SKLIEY) is a substrate of NatA and is derived from the protein endoded by tsaE/Rv3422c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-seryl-[KLIEY]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[KLIEY]
DP6 peptide (SKLIEY) is a substrate of NatA and is derived from the protein endoded by tsaE/Rv3422c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-seryl-[RVQIS]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[RVQIS]
DP4 peptide (SRVQIS) is a substrate of NatA and is derived from the protein endoded by tsaB/Rv3421c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-seryl-[RVQIS]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[RVQIS]
DP4 peptide (SRVQIS) is a substrate of NatA and is derived from the protein endoded by tsaB/Rv3421c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + N-terminal L-seryl-[RVQIS]
CoA + H+ + N-terminal Nalpha-acetyl-L-seryl-[RVQIS]
DP4 peptide (SRVQIS) is a substrate of NatA and is derived from the protein endoded by tsaB/Rv3421c (Mtb), a neighboring non-ribosomal protein
-
-
ir
acetyl-CoA + Orc1p
CoA + Nalpha-acetyl-[Orc1p]
-
-
-
-
?
acetyl-CoA + Orc1p
CoA + Nalpha-acetyl-[Orc1p]
-
Orc1p is the large subunit of the origin recognition complex, ORC. Mechanism for modulating chromaffin function
-
-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
-
-
-
-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
-
NatA acetylation is important for function of a set of proteins involved in general groth control
-
-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
-
acetylates N-terminal Ser, Ala, Gly or Thr residues
-
-
?
acetyl-CoA + peptide
Nalpha-acetylpeptide + CoA
-
-
-
-
?
acetyl-CoA + peptide
Nalpha-acetylpeptide + CoA
-
-
-
-
?
acetyl-CoA + silencing facor Sir3p
CoA + Nalpha-acetyl-[silencing factor Sir3p]
-
-
-
-
?
acetyl-CoA + silencing facor Sir3p
CoA + Nalpha-acetyl-[silencing factor Sir3p]
-
mechanism for modulating chromaffin function
-
-
?
acetyl-CoA + [Runx2]
[Runx2]-N-terminal-N6-acetyl-L-lysine + CoA
-
-
-
-
?
acetyl-CoA + [Runx2]
[Runx2]-N-terminal-N6-acetyl-L-lysine + CoA
NAA10 acetylates Runx2 at Lys225
-
-
?
additional information
?
-
N-terminal EEEI is acetylated 3fold more than the DDDI substrate, which again is preferred almost 2fold to SESS, the canonical NatA substrate
-
-
?
additional information
?
-
-
N-terminal EEEI is acetylated 3fold more than the DDDI substrate, which again is preferred almost 2fold to SESS, the canonical NatA substrate
-
-
?
additional information
?
-
enzyme zNaa10 has a predicted N-terminal activity with identical substrate specificity to human Naa10 in vitro
-
-
-
additional information
?
-
-
endogenous HYPK, a Huntingtin (Htt)-interacting protein, is a stable interactor of NatA, the C terminus of hNaa15p of NatA specifically interacts directly with HYPK, no interaction with hNaa25p of hNatB and hNaa35p of hNatC
-
-
?
additional information
?
-
enzyme variant ARD1131 has no autoacetylation activity
-
-
?
additional information
?
-
-
N-terminal acetyltransferase Naa10/ARD1 does not acetylate lysine residues
-
-
?
additional information
?
-
Naa10 undergoes autoacetylation at lysine K136
-
-
?
additional information
?
-
lysine acetyltransferase (KAT) activity of recombinant human ARD1/NAA10, overview. Arrest defective 1 (ARD1) is the only enzyme known so far to exhibit both N-terminal acetyltransferase (NAT) and N-terminal lysine acetyltransferase (KAT) activities. Only the monomeric rhARD1/NAA10 form, but not by the oligomeric form, can acetylate lysine residues of substrate proteins
-
-
-
additional information
?
-
N-terminal acetylation (NTA) is an irreversible protein modification
-
-
-
additional information
?
-
no activity with an MMP2 mutated at the acetylytion site of Naa10
-
-
-
additional information
?
-
recombinant hARD1/NAA10 exhibits KAT activity, which disappears soon in vitro due to enzyme oligomerization, which results in the loss of KAT activity. While oligomeric recombinant hARD1/NAA10 loses its ability for lysine acetylation, its monomeric form clearly exhibits lysine acetylation activity in vitro. Assay optimization, under optimal conditions, hARD1/NAA10 retains its KAT activity, overview
-
-
-
additional information
?
-
substrates are SESS24 or EEEI24. The ability of NAA10-V111G to acetylate the acidic N-termini EEEI24 is highly reduced compared to wild-type enzyme
-
-
-
additional information
?
-
-
substrates are SESS24 or EEEI24. The ability of NAA10-V111G to acetylate the acidic N-termini EEEI24 is highly reduced compared to wild-type enzyme
-
-
-
additional information
?
-
ARD1 and NAT1 constitute an N-acetyltransferase complex where ARD1 holds the enzymatic activity of the complex. The ARD1-NAT1 complex mediates N-terminal acetylation of nascent polypeptides that emerge from ribosomes after translation. ARD1 may also acetylate the internal lysine residues of proteins
-
-
?
additional information
?
-
acetylation of alpha-tubulin
-
-
-
additional information
?
-
acetylation of alpha-tubulin
-
-
-
additional information
?
-
acetylation of alpha-tubulin
-
-
-
additional information
?
-
acetylation of alpha-tubulin
-
-
-
additional information
?
-
analysis of substrate preference of RimIMtb: substrate peptide DPC (NatA substrate) is custom synthesized with single residue modifications at its N-terminus to represent substrate specificities of NatE (DP9), NatB (DP10), NatC (DP11), and substrate Leu (DP8) and tested, all the peptides are modified by RimIMtb, substrates and sequences, detailed overview. RimIMtb acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins. The NatB substrate peptide MERYFRR is a poor substrate for RimI. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed against peptide representing N-terminus of GroES
-
-
-
additional information
?
-
-
analysis of substrate preference of RimIMtb: substrate peptide DPC (NatA substrate) is custom synthesized with single residue modifications at its N-terminus to represent substrate specificities of NatE (DP9), NatB (DP10), NatC (DP11), and substrate Leu (DP8) and tested, all the peptides are modified by RimIMtb, substrates and sequences, detailed overview. RimIMtb acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins. The NatB substrate peptide MERYFRR is a poor substrate for RimI. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed against peptide representing N-terminus of GroES
-
-
-
additional information
?
-
the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE). RimIMtb acetylates DP9 (NatE substrate) 18fold better than DPC (NatA substrate)
-
-
-
additional information
?
-
-
the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE). RimIMtb acetylates DP9 (NatE substrate) 18fold better than DPC (NatA substrate)
-
-
-
additional information
?
-
the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE). RimIMtb acetylates DP9 (NatE substrate) 18fold better than DPC (NatA substrate)
-
-
-
additional information
?
-
analysis of substrate preference of RimIMtb: substrate peptide DPC (NatA substrate) is custom synthesized with single residue modifications at its N-terminus to represent substrate specificities of NatE (DP9), NatB (DP10), NatC (DP11), and substrate Leu (DP8) and tested, all the peptides are modified by RimIMtb, substrates and sequences, detailed overview. RimIMtb acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins. The NatB substrate peptide MERYFRR is a poor substrate for RimI. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed against peptide representing N-terminus of GroES
-
-
-
additional information
?
-
the bifunctional enzyme RimI exhibits activity of EC 2.3.1.255 (NatA) and EC 2.3.1.258 (NatE). RimIMtb acetylates DP9 (NatE substrate) 18fold better than DPC (NatA substrate)
-
-
-
additional information
?
-
analysis of substrate preference of RimIMtb: substrate peptide DPC (NatA substrate) is custom synthesized with single residue modifications at its N-terminus to represent substrate specificities of NatE (DP9), NatB (DP10), NatC (DP11), and substrate Leu (DP8) and tested, all the peptides are modified by RimIMtb, substrates and sequences, detailed overview. RimIMtb acetylates N-terminus of ribosomal proteins and of neighboring non-ribosomal proteins. The NatB substrate peptide MERYFRR is a poor substrate for RimI. RimIMtb does acetylate peptides representing N-terminus of GroES, GroEL1, and TsaD proteins, in vitro. Significant specific activity of RimIMtb is observed against peptide representing N-terminus of GroES
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additional information
?
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both proteins ARD1 and NAT1 are required for the N-terminal acetyltransferase activity of the ARD1-NAT1 complex
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?
additional information
?
-
typical NatA (Naa10) substrates all start with small amino acids (alanine, serine, threonine, or valine) after excision of methionine. N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
?
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-
typical NatA (Naa10) substrates all start with small amino acids (alanine, serine, threonine, or valine) after excision of methionine. N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
?
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typical NatA (Naa10) substrates all start with small amino acids (alanine, serine, threonine, or valine) after excision of methionine. N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
?
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N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
?
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N-terminal acetylation (NTA) is an irreversible protein modification
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additional information
?
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N-terminal acetylation (NTA) is an irreversible protein modification
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acetyl-CoA + an N-terminal-amino acid-[protein]
an N-terminal-Nalpha-acetyl-amino acid-[protein] + CoA
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-
-
?
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
acetyl-CoA + an N-terminal-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-valyl-[protein] + CoA
acetyl-CoA + an N-terminal-lysinyl-[androgen receptor]
an N-terminal-Nalpha-acetyl-lysinyl-[androgen receptor] + CoA
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ARD1 acetylates androgen receptor at lysine 618
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-
?
acetyl-CoA + an N-terminal-methionyl-[RPM1 protein]
an N-terminal-Nalpha-acetyl-methionyl-[RPM1 protein] + CoA
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-
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-
?
acetyl-CoA + an N-terminal-methionyl-[SNC1 protein]
an N-terminal-Nalpha-acetyl-methionyl-[SNC1 protein] + CoA
-
NatA specifically acetylates the first met of SNC1 protein
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?
acetyl-CoA + beta-catenin
?
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?
acetyl-CoA + DDDIAAL
CoA + N-acetyl-DDDIAAL
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-
-
?
acetyl-CoA + EEEIAAL
CoA + N-acetyl-EEEIAAL
best substrate
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-
?
acetyl-CoA + MLGPEGG
CoA + N-acetyl-MLGPEGG
poor substrate
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-
?
acetyl-CoA + Orc1p
CoA + Nalpha-acetyl-[Orc1p]
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Orc1p is the large subunit of the origin recognition complex, ORC. Mechanism for modulating chromaffin function
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?
acetyl-CoA + PCNP protein
CoA + Nalpha-acetyl-PCNP protein
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i.e. PEST proteolytic signal-containing nuclear protein
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-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
acetyl-CoA + peptide
Nalpha-acetylpeptide + CoA
acetyl-CoA + SESSSKS
CoA + N-acetyl-SESSSKS
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-
-
?
acetyl-CoA + silencing facor Sir3p
CoA + Nalpha-acetyl-[silencing factor Sir3p]
-
mechanism for modulating chromaffin function
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?
acetyl-CoA + [histone 2B]
an N-terminal-Nalpha-acetyl-[histone 2B] + CoA
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-
-
-
?
acetyl-CoA + [iso-1-cytochrome c]
an N-terminal-Nalpha-acetyl-[iso-1-cytochrome c] + CoA
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-
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?
acetyl-CoA + [Runx2]
[Runx2]-N-terminal-N6-acetyl-L-lysine + CoA
NAA10 acetylates Runx2 at Lys225
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-
?
additional information
?
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endogenous HYPK, a Huntingtin (Htt)-interacting protein, is a stable interactor of NatA, the C terminus of hNaa15p of NatA specifically interacts directly with HYPK, no interaction with hNaa25p of hNatB and hNaa35p of hNatC
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-
?
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
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-
-
-
?
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-glycyl-[protein]
an N-terminal-Nalpha-acetyl-glycyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-alanyl-[protein]
an N-terminal-Nalpha-acetyl-L-alanyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-cysteinyl-[protein]
an N-terminal-Nalpha-acetyl-L-cysteinyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-seryl-[protein]
an N-terminal-Nalpha-acetyl-L-seryl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
-
-
-
-
?
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-threonyl-[protein]
an N-terminal-Nalpha-acetyl-L-threonyl-[protein] + CoA
-
-
-
?
acetyl-CoA + an N-terminal-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-valyl-[protein] + CoA
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-
-
-
?
acetyl-CoA + an N-terminal-L-valyl-[protein]
an N-terminal-Nalpha-acetyl-L-valyl-[protein] + CoA
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-
-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
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-
-
-
?
acetyl-CoA + peptide
CoA + Nalpha-acetylpeptide
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NatA acetylation is important for function of a set of proteins involved in general groth control
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?
acetyl-CoA + peptide
Nalpha-acetylpeptide + CoA
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-
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?
acetyl-CoA + peptide
Nalpha-acetylpeptide + CoA
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-
-
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?
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evolution
RimI belongs to the general control non-repressible (GCN5)-related N-acetyltransferase (GNAT) family that carries a conserved Q/RxxGxG/A Ac-CoA-binding motif
evolution
there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.)
evolution
there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.)
evolution
there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.)
evolution
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there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.)
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evolution
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there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.)
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evolution
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there are seven known NAT types (NatA through NatG), each composed of one or more specific subunits and having specific substrates defined by the very first amino acid residue (serine, alanine, etc.)
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evolution
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RimI belongs to the general control non-repressible (GCN5)-related N-acetyltransferase (GNAT) family that carries a conserved Q/RxxGxG/A Ac-CoA-binding motif
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evolution
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RimI belongs to the general control non-repressible (GCN5)-related N-acetyltransferase (GNAT) family that carries a conserved Q/RxxGxG/A Ac-CoA-binding motif
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malfunction
Aenzyme knockdown significantly reduces dendritic extension in cultured Purkinje cells
malfunction
-
knockdown of acetyltransferase ARD1 significantly reduces the growth rate of human cancer cell lines. Furthermore, ARD1 knockdown induces apoptosis or sensitizes cells to drug induced apoptosis. Enzyme knockdown reduces the transcriptional activity of the beta-Catenin/TCF4 complex, downregulating cyclin D1 and thereby promoting G1-arrest and inhibition of cell proliferation of lung cancer cells
malfunction
knockdown of Naa10 in HeLa cells leads to apoptosis and sensitizes cells for daunorubicin-induced apoptosis
malfunction
mutations in N-terminal acetyltransferase Naa10 are the cause of Ogden Syndrome
malfunction
naa10 morphants display increased lethality, growth retardation and developmental abnormalities like bent axis, abnormal eyes and bent tails
malfunction
reduced enzyme levels result in pleiotropic oogenesis defects including abnormal cyst encapsulation, desynchronized cystocyte division, disrupted nurse cell chromosome dispersion, and abnormal chorion patterning. Loss of Ard1 affects cell survival/proliferation and is lethal for the animal
malfunction
enzyme knockdown causes a phenotype with lethality, growth retardation, bent axis and tails, abnormal eyes, and less pigmentation
malfunction
enzyme mutants show phenotypes with pleiotropic oogenesis, aberrant mitosis, egg chamber encapsulation defects, and nurse cell chromatin dispersion defects
malfunction
HYPK is a negative regulator for hNatA acetylation activity
malfunction
inactive Naa10 mutant S37Pw shows a phenotype with perinatal lethal disorder, hypotonia, global developmental delay, cryptorchidism, cardiac arrhythmias, skin laxity, dysmorphic features, hernias, and large fontanels. Naa10 mutant Y43S shows a phenotype with intellectual disability, facial dysmorphism, scoliosis, and long QT. Mutant R83C shows a phenootype with hypotonia, global developmental delay, dysmorphic features, autism spectrum disorder, epileptic encephalopathy, extrapyramidal signs, hypertension with left ventricular hypertrophy, thin corpus callosum, and progressive white matter loss. Mutations V107F and R116W cause phenotypes with severe global developmental delay with postnatal growth, skeletal anomalies, truncal hypotonia with hypertonia of the extremities, minor facial features, and behavioral anomalies. Mutation of residue F128 causes moderate to severe intellectually disability, feeding difficulties, eye anomalies, hypotonia, and developmental delay
malfunction
inhibition of hARD1/NAA10 autoacetylation by K136R mutation induces the drop of KAT activity, but not NAT activity
malfunction
knockdown and overexpression of Naa10p in osteosarcoma cells respectively leads to decreased and increased cell migratory/invasive abilities. Re-expression of Naa10p, but not of an enzymatically inactive mutant, relieves suppression of the invasive ability in vitro and metastasis in vivo imposed by Naa10p-knockdown. The matrix metalloproteinase (MMP)-2 is responsible for the Naa10p-induced invasive phenotype
malfunction
measuring the different time points of gene expression upon Naa10 siRNA treatment, NTN1 and its receptor UNC5B are found to be the most dramatically overexpressed among the genes involved in morphogenesis
malfunction
measuring the different time points of gene expression upon Naa10 siRNA treatment, NTN1 and its receptor UNC5B are found to be the most dramatically overexpressed among the genes involved in morphogenesis. Analysis of upregulated genes in Naa10 stably knocked down H1299 cell line, overview
malfunction
mutation ard1::HIS3 leads to a defect in transcription of a-specific genes, but permits expression of the information resident at HML. The mutant shows a phenotypes with reduced viability and sensitivity to heat shock and salt, it fails to enter stationay phase, it shows a lack of glycogen accumulation, a sporulation defect, poor mating, and fails to undergo meiosis. The mutant nat1-5::LEU;ard1 is inable to sporulate, has slow growth, reduced mating, inhibited sporulation, and impaired resistance to heat shock. It fails G1 arrest, shows a partial depression of HML, and fails to accumulate storage. yNaa10 deficiency leads to a growth defect, sensitivity to caffeine and cycloheximide, impaired resistance to heat shock, and decreased mating efficiency
malfunction
mutations in the X-linked gene NAA10 cause Ogden Syndrome (also known as NAA10-related syndrome), which affects numerous aspects of development. Wide-ranging developmental defects are observed in humans with mutations in NAA10 and NAA15
malfunction
NAA10 germline variants are found in patients with the X-linked lethal Ogden syndrome, and in other familial or de novo cases with variable degrees of developmental delay, intellectual disability (ID) and cardiac anomalies. A R83H missense variant in NAA10 is detected by whole exome sequencing in two unrelated boys with intellectual disability, developmental delay, ADHD like behaviour, very limited speech and cardiac abnormalities. Phenotypes, overview. Mutant NAA10-R83H has a reduced monomeric catalytic activity, likely due to impaired enzyme-acetyl-CoA binding
malfunction
NAA10 variants have been found in patients with an X-linked developmental disorder called Ogden syndrome in its most severe form and, in other familial or de novo cases, with variable degrees of syndromic intellectual disability (ID) affecting both sexes. The mutant NAA10-V111G has a reduced stability and 85% reduced monomeric catalytic activity, while catalytic NatA function remains unaltered. The syndromic cases may also require a degree of compromised NatA function. The Naa10-V111G phenotype shows mild/moderate non-syndromic intellectual disability, and delayed motor and language development, but normal behavior without autistic traits. The blood leukocyte X-inactivation pattern is within normal range (80/20)
malfunction
oligomerization results in the loss of KAT activity
malfunction
overexpression of gene daf-31 causes an increased lifespan in daf-2 mutant enhancing reproduction, while daf-31 knockdown by siRNA causes a decreased lifespan
malfunction
overexpression of Naa10 in mice results in the delayed closure of calvarial fontanels and reduced bone density, osteoblast surfaces and mRNA levels of the osteoblastogenic genes in calvaria. In contrast, Naa10 deficient mice display calvarial and femoral bone development to a greater extent on postnatal day 3
malfunction
several X-linked NAA10 variants have been associated with genetic disorders. A NAA10 variant I72T with impaired acetyltransferase activity causes developmental delay, intellectual disability, and hypertrophic cardiomyopathy. Genotype-phenotype correlations for NAA10 variants, overview
malfunction
the ARD1 null mutation leads to impaired growth in bloodstream-form cells and reduced differentiation to insect-stage cells
malfunction
the naa10 knockout mutant naa10-1 shows growth retardation in vegetative stage, abortion of embryogenesis, and drought-adapted root morphology, the mutation is lethal. A knockout of naa15 causes the same phenotype
malfunction
-
overexpression of Naa10 in mice results in the delayed closure of calvarial fontanels and reduced bone density, osteoblast surfaces and mRNA levels of the osteoblastogenic genes in calvaria. In contrast, Naa10 deficient mice display calvarial and femoral bone development to a greater extent on postnatal day 3
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malfunction
-
mutations in the X-linked gene NAA10 cause Ogden Syndrome (also known as NAA10-related syndrome), which affects numerous aspects of development. Wide-ranging developmental defects are observed in humans with mutations in NAA10 and NAA15
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malfunction
-
mutation ard1::HIS3 leads to a defect in transcription of a-specific genes, but permits expression of the information resident at HML. The mutant shows a phenotypes with reduced viability and sensitivity to heat shock and salt, it fails to enter stationay phase, it shows a lack of glycogen accumulation, a sporulation defect, poor mating, and fails to undergo meiosis. The mutant nat1-5::LEU;ard1 is inable to sporulate, has slow growth, reduced mating, inhibited sporulation, and impaired resistance to heat shock. It fails G1 arrest, shows a partial depression of HML, and fails to accumulate storage. yNaa10 deficiency leads to a growth defect, sensitivity to caffeine and cycloheximide, impaired resistance to heat shock, and decreased mating efficiency
-
malfunction
-
overexpression of gene daf-31 causes an increased lifespan in daf-2 mutant enhancing reproduction, while daf-31 knockdown by siRNA causes a decreased lifespan
-
malfunction
-
measuring the different time points of gene expression upon Naa10 siRNA treatment, NTN1 and its receptor UNC5B are found to be the most dramatically overexpressed among the genes involved in morphogenesis
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metabolism
ARD1 variants have different effects on hypoxia-inducible factor-1alpha stability and acetylation
metabolism
ARD1 variants have different effects on hypoxia-inducible factor-1alpha stability and acetylation
metabolism
Naa10 activates and/or amplifies the transcriptional activity of beta-catenin/TCF transcriptional activity thereby stimulating cyclin D1 and c-Myc expression leading to inhibition of p21WAF1/CIP1 and promoting the G1/S cell cycle transition. Naa10 is essential for the activation of caspase-2/-3/-7 and -9 in HeLa cells after doxorubicin stimulation
metabolism
-
NAT1 and ARD1 proteins function together to catalyze the N-terminal acetylation of a subset of yeast proteins
metabolism
the enzyme is involved in the co-translational N-terminal protein modification process, overview
metabolism
the enzyme is involved in the co-translational N-terminal protein modification process, overview
metabolism
the enzyme is involved in the co-translational N-terminal protein modification process, overview
metabolism
-
the enzyme is involved in the co-translational N-terminal protein modification process, overview
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metabolism
-
the enzyme is involved in the co-translational N-terminal protein modification process, overview
-
metabolism
-
the enzyme is involved in the co-translational N-terminal protein modification process, overview
-
physiological function
ARD1 is essential for viability in mammalian and insect-stage Trypanosoma brucei cells
physiological function
enzyme variant ARD1131 has no influence on cyclin D1 expression and cell growth
physiological function
the ARD1-NAT1 complex has acetyltransferase activity against microtubules in dendrites and regulates dendritic arborization in neuronal cells
physiological function
-
the enzyme acts in complex with the NATH protein and catalyzes cotranslational acetylation of protein N-termini
physiological function
the enzyme controls osteoblast differentiation and bone formation as a feedback regulator of Runt-related transcription factor 2
physiological function
the enzyme is essential for normal development and viability of zebrafish
physiological function
-
the enzyme is involved in ribosome synthesis. Optimal NatA function is important to the cooperative function of Brx1 with Ebp2 in 60S ribosomal subunit biogenesis
physiological function
arrest defective 1 (ARD1), also known as N(alpha)-acetyltransferase 10 (NAA10) is originally identified as an N-terminal acetyltransferase (NAT) that catalyzes the acetylation of N-termini of newly synthesized peptides. Mammalian ARD1/NAA10 also plays a role as lysine acetyltransferase (KAT) that posttranslationally acetylates internal lysine residues of proteins. ARD1/NAA10 is the only enzyme with both NAT (EC 2.3.1.255) and KAT (EC 2.3.1.48) activities. NATs acetylate N-terminal residues of newly synthesized proteins from ribosomes in an irreversible manner. N-terminal acetylation is known to be closely related to protein stability, interaction, and localization. lysine acetylation catalyzed by KATs is reversibly regulated by lysine deacetyltransferases (KDACs) that remove acetyl groups from lysine residues in proteins. While acetylation neutralizes the positive charge on lysine residues, deacetylation recovers it, thereby causing a change in electronic and conformational properties of proteins. Acetylation and deacetylation of lysine residues serve as the switches that turn-on and turn-off the cellular signal pathways and regulate diverse biological events. Any unbalance between lysine acetylation and deacetylation results in the improper regulation of biological processes and may cause various types of human diseases such as cancer and neurodegeneration
physiological function
enzyme Daf-31 regulates the transcriptional activity of DAF-16, the FOXO transcription factor. Mutant daf-31(m655) leads to developmental larval arrest, fat accumulation, formation of dauer-like larvae under starvation conditions, and decreased lifespan, and the mutant lacks SDS-resistance and cannot resume development and reproduction after food re-providing
physiological function
hNatA significantly enhances the catalytic efficiency of hNatE (EC 2.3.1.258). The hNatE complex comprises subunits Naa10 and Naa15 (NatA) and Naa50. HYPK binding to hNatE largely nullifies this effect
physiological function
importance of NAA10 catalytic activity in human development. The potential role of NAA10 varies depending on transcriptional levels in different tissues and embryonic stages during development
physiological function
importance of NAA10 catalytic activity in mouse development. The potential role of NAA10 varies depending on transcriptional levels in different tissues and embryonic stages during development. Naa10 homologue Naa11 has a role in the cellular differentiation process while Naa10 has a role in the cellular proliferation process. The differential expression pattern of Naa10 and Naa11 suggests that Naa11 is complementary to Naa10 at least in the mice and that its biological role can be important in spermiogenesis or cellular processes
physiological function
importance of NAA10 catalytic activity in mouse development. The potential role of NAA10 varies depending on transcriptional levels in different tissues and embryonic stages during development. Naa10 homologue Naa11 has a role in the cellular differentiation process while Naa10 has a role in the cellular proliferation process. The differential expression pattern of Naa10 and Naa11 suggests that Naa11 is complementary to Naa10 at least in the mice and that its biological role can be important in spermiogenesis or cellular processes. Naa10 is known to regulate cellular processes, and its effects are not only catalyzed through its major activity as a NAT but also through the N-epsilon-acetylation of several proteins. The N-epsilon-acetyl-activity of Naa10 requires auto-acetylation. This requirement is similar to that of other acetyltransferases, which acetylate themselves for their catalytic and functional activities. Naa10 plays an important role in osteoblast differentiation and the early phases of bone formation. Naa10 counteracts HDAC6 by acetylating alpha-tubulin, thereby promoting MT stability for dendritic development
physiological function
N-alpha-acetyltransferase 10 (Naa10) is the catalytic subunit of N-acetyltransferase A (NatA), it catalyzes N-alpha-acetylation, epsilon-acetylation, as well as autoacetylation. The alpha (N-terminal) acetyltransferase functions as a major modulator of cell growth and differentiation. Potential function of Naa10 in cell morphogenesis. Negative regulation of Naa10 towards NTN1 and its receptor UNC5B are detected upon treatment of all-trans retinoid acid, used to induce morphological differentiation. UNC-5 Homolog B (UNC5b), a dependence receptor of netrin-1, plays an essential role in mediating the repulsive effect of axonal migration and blood vessel formation through association with its ligand netrin-1 (NTN1). In addition, UNC5B has also been indicated as a putative tumor suppressor gene in numerous cancers
physiological function
N-alpha-acetyltransferase 10 (Naa10) is the catalytic subunit of N-acetyltransferase A (NatA), it catalyzes N-alpha-acetylation, epsilon-acetylation, as well as autoacetylation. The alpha (N-terminal) acetyltransferase functions as a major modulator of cell growth and differentiation. Potential function of Naa10 in cell morphogenesis. Negative regulation of Naa10 towards NTN1 and its receptor UNC5B are detected upon treatment of all-trans retinoid acid, usedto induce morphological differentiation. UNC-5 Homolog B (UNC5b), a dependence receptor of netrin-1, plays an essential role in mediating the repulsive effect of axonal migration and blood vessel formation through association with its ligand netrin-1 (NTN1). In addition, UNC5B has also been indicated as a putative tumor suppressor gene in numerous cancers
physiological function
N-alpha-acetyltransferase 10 protein (Naa10p) mediates N-terminal acetylation of nascent proteins. It promotes metastasis by stabilizing matrix metalloproteinase-2 protein in human osteosarcomas via its N-terminal acetylation activity. Oncogenic role of Naa10p, overview. Higher NAA10 transcripts are observed in metastatic osteosarcoma tissues compared to non-metastatic tissues and are also correlated with a worse prognosis of patients. Naa10p is directly associated with MMP-2 protein through its acetyltransferase domain and maintains MMP-2 protein stability via NatA complex activity. MMP-2 expression levels are also significantly correlated with Naa10p levels in osteosarcoma tissues. Function of Naa10p in the regulation of cell invasiveness by preventing MMP-2 protein degradation that is crucial during osteosarcoma metastasis. Naa10p promotes migratory/invasive abilities of osteosarcoma cells, it regulates cell invasion of the osteosarcoma cell lines
physiological function
N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification
physiological function
N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification
physiological function
N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is estimated to affect up to 90% of human proteins and influences their folding, localization, complex formation, and degradation, along with a variety of cellular functions ranging from apoptosis to gene regulation. NTA is an irreversible protein modification
physiological function
N-terminal acetylation catalyzed by NATs is one of the most common protein modifications in eukaryotes, affecting about 80% human proteins. In general, NATs acetylate N-terminal residues of newly synthesized proteins from ribosomes in an irreversible manner. N-terminal acetylation is known to be closely related to protein stability, interaction, and localization. Human ARD1/NAA10 expanded its' role to lysine acetyltransferase (KAT) that post-translationally acetylates internal lysine residues of proteins. Size-exclusion analysis reveals that most recombinant hARD1/NAA10 forms oligomers While oligomeric recombinant hARD1/NAA10 loses its ability for lysine acetylation, its monomeric form clearly exhibited lysine acetylation activity in vitro. In contrast to N-terminal acetylation, lysine acetylation catalyzed by KATs is reversibly regulated by lysine deacetyltransferases (KDACs) that remove acetyl groups from lysine residues in protein. hARD1 regulates a wide range of cellular functions, including cell cycle, apoptosis, migration, stress response, and differentiation. NAT and KAT activity might be independently regulated, relying on the interaction partners
physiological function
N-terminal acetylation is a common protein modification in human cells and is catalysed by N-terminal acetyltransferases (NATs), mostly cotranslationally. The NAA10-NAA15 (NatA) protein complex is the major NAT, responsible for acetylating about 40% of human protein. Naa15 is the NatA auxiliary subunit
physiological function
Naa10 is crucial for cell growth and sporulation
physiological function
Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs)
physiological function
RimI, an Nalpha-acetyltransferase in Mycobacterium tuberculosis, is responsible for the acetylation of the alpha-amino group of the N-terminal residue in the ribosomal protein S18. Protein acetylation may be correlated with the pathogenesis of tuberculosis
physiological function
Q4DSU6; Q4D0P4
TcNatC/TcNatA proteins carry out their function independently of each other as suggested in other organisms and they may have specific functions depending on the parasite life cycle stage. But the proteins may also have other functions independent of the NAT-activity as suggested in other species
physiological function
the NAA10-NAA15 (NatA) protein complex is an N-terminal acetyltransferase responsible for acetylating about of eukaryotic proteins
physiological function
the NAA10-NAA15 complex (NatA) is an N-terminal acetyltransferase that catalyzes N-terminal acetylation of about 40% of all human proteins. N-terminal acetylation has several different roles in the cell, including altering protein stability and degradation, protein localization and protein-protein interactions
physiological function
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N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification
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physiological function
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TcNatC/TcNatA proteins carry out their function independently of each other as suggested in other organisms and they may have specific functions depending on the parasite life cycle stage. But the proteins may also have other functions independent of the NAT-activity as suggested in other species
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physiological function
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N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification
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physiological function
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importance of NAA10 catalytic activity in mouse development. The potential role of NAA10 varies depending on transcriptional levels in different tissues and embryonic stages during development. Naa10 homologue Naa11 has a role in the cellular differentiation process while Naa10 has a role in the cellular proliferation process. The differential expression pattern of Naa10 and Naa11 suggests that Naa11 is complementary to Naa10 at least in the mice and that its biological role can be important in spermiogenesis or cellular processes
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physiological function
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importance of NAA10 catalytic activity in mouse development. The potential role of NAA10 varies depending on transcriptional levels in different tissues and embryonic stages during development. Naa10 homologue Naa11 has a role in the cellular differentiation process while Naa10 has a role in the cellular proliferation process. The differential expression pattern of Naa10 and Naa11 suggests that Naa11 is complementary to Naa10 at least in the mice and that its biological role can be important in spermiogenesis or cellular processes. Naa10 is known to regulate cellular processes, and its effects are not only catalyzed through its major activity as a NAT but also through the N-epsilon-acetylation of several proteins. The N-epsilon-acetyl-activity of Naa10 requires auto-acetylation. This requirement is similar to that of other acetyltransferases, which acetylate themselves for their catalytic and functional activities. Naa10 plays an important role in osteoblast differentiation and the early phases of bone formation. Naa10 counteracts HDAC6 by acetylating alpha-tubulin, thereby promoting MT stability for dendritic development
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physiological function
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N-terminal acetylation (NTA) is among the most widespread co-translational modifications found in eukaryotic proteins. NTA is carried out by N-terminal acetyltransferases (NATs), which catalyze the transfer of an acetyl moiety from acetyl coenzyme A to the N-terminal amino group of the nascent polypeptides as they emerge from the ribosome. NTA is an irreversible protein modification
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physiological function
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Naa10 is crucial for cell growth and sporulation
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physiological function
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RimI, an Nalpha-acetyltransferase in Mycobacterium tuberculosis, is responsible for the acetylation of the alpha-amino group of the N-terminal residue in the ribosomal protein S18. Protein acetylation may be correlated with the pathogenesis of tuberculosis
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physiological function
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Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs)
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physiological function
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enzyme Daf-31 regulates the transcriptional activity of DAF-16, the FOXO transcription factor. Mutant daf-31(m655) leads to developmental larval arrest, fat accumulation, formation of dauer-like larvae under starvation conditions, and decreased lifespan, and the mutant lacks SDS-resistance and cannot resume development and reproduction after food re-providing
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physiological function
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RimI, an Nalpha-acetyltransferase in Mycobacterium tuberculosis, is responsible for the acetylation of the alpha-amino group of the N-terminal residue in the ribosomal protein S18. Protein acetylation may be correlated with the pathogenesis of tuberculosis
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physiological function
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Nalpha-acetylation is a naturally occurring irreversible modification of N-termini of proteins catalyzed by Nalpha-acetyltransferases (NATs)
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physiological function
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N-alpha-acetyltransferase 10 (Naa10) is the catalytic subunit of N-acetyltransferase A (NatA), it catalyzes N-alpha-acetylation, epsilon-acetylation, as well as autoacetylation. The alpha (N-terminal) acetyltransferase functions as a major modulator of cell growth and differentiation. Potential function of Naa10 in cell morphogenesis. Negative regulation of Naa10 towards NTN1 and its receptor UNC5B are detected upon treatment of all-trans retinoid acid, usedto induce morphological differentiation. UNC-5 Homolog B (UNC5b), a dependence receptor of netrin-1, plays an essential role in mediating the repulsive effect of axonal migration and blood vessel formation through association with its ligand netrin-1 (NTN1). In addition, UNC5B has also been indicated as a putative tumor suppressor gene in numerous cancers
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physiological function
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ARD1 is essential for viability in mammalian and insect-stage Trypanosoma brucei cells
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additional information
NatA homology modeling. Residue V111 is located towards the end of the beta5 strand, and a valine in this position is highly conserved in NAA10 homologues as well as in several other NAT catalytic subunits for which crystal structures have been solved. The side chain of V111 is forming a hydrophobic pocket together with Y145, M147, L119 and L109. It is also in close proximity to the sulfur group of acetyl-CoA, which seems to indicate a role for V111 in positioning of acetyl-CoA. A glycine in this position will not cause any steric clashes, but loss of the more bulky hydrophobic side chain of valine may possibly cause structural alterations affecting protein stability or AcCoA binding
additional information
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NatA homology modeling. Residue V111 is located towards the end of the beta5 strand, and a valine in this position is highly conserved in NAA10 homologues as well as in several other NAT catalytic subunits for which crystal structures have been solved. The side chain of V111 is forming a hydrophobic pocket together with Y145, M147, L119 and L109. It is also in close proximity to the sulfur group of acetyl-CoA, which seems to indicate a role for V111 in positioning of acetyl-CoA. A glycine in this position will not cause any steric clashes, but loss of the more bulky hydrophobic side chain of valine may possibly cause structural alterations affecting protein stability or AcCoA binding
additional information
structure comparison, wild-type NAA10 and mutant NAA10-R83H from the human NatA complex (PDB ID 6C9M) are compared with the structure of NAA10 from the Schizosaccharomyces pombe NatA complex (PDB ID 4KVM)
additional information
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structure comparison, wild-type NAA10 and mutant NAA10-R83H from the human NatA complex (PDB ID 6C9M) are compared with the structure of NAA10 from the Schizosaccharomyces pombe NatA complex (PDB ID 4KVM)
additional information
structure modeling and molecular docking of RimI, docking of the structure model of MtRimI-Ala-Arg-Tyr-Phe-Arg-Arg (ARYFRR) complex using the crystal structure of the RimI and bisubstrate from Salmonella typhimurium strain LT2 (PDB 2CNM) as template, overview. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
additional information
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structure modeling and molecular docking of RimI, docking of the structure model of MtRimI-Ala-Arg-Tyr-Phe-Arg-Arg (ARYFRR) complex using the crystal structure of the RimI and bisubstrate from Salmonella typhimurium strain LT2 (PDB 2CNM) as template, overview. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
additional information
the NAT activity is highest for the monomeric enzyme, about 2fold higher compared to the oligomeric enzyme and about 20% higher compared to the dimeric enzyme
additional information
the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures
additional information
the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures, and ScNaa10 is similarly and completely locked into a cradle by the surrounding Naa15 helices. ScNaa50 has a robust interaction with ScNatA that is maintained even in high salt concentrations (1 M NaCl)
additional information
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the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures, and ScNaa10 is similarly and completely locked into a cradle by the surrounding Naa15 helices. ScNaa50 has a robust interaction with ScNatA that is maintained even in high salt concentrations (1 M NaCl)
additional information
the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures. SpNaa50 has a robust interaction with SpNatA that is maintained even in high salt concentrations (1 M NaCl)
additional information
Q4DSU6; Q4D0P4
Trypanosoma cruzi NatA protein complex consists of one catalytic subunit and one predicted auxiliary subunit. TcNatC (EC 2.3.1.256) and TcNatA complex subunits interact in vivo and in vitro
additional information
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the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures. SpNaa50 has a robust interaction with SpNatA that is maintained even in high salt concentrations (1 M NaCl)
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additional information
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Trypanosoma cruzi NatA protein complex consists of one catalytic subunit and one predicted auxiliary subunit. TcNatC (EC 2.3.1.256) and TcNatA complex subunits interact in vivo and in vitro
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additional information
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the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures. SpNaa50 has a robust interaction with SpNatA that is maintained even in high salt concentrations (1 M NaCl)
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additional information
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the NatA enzyme complex is composed of the subunits Naa10 and Naa15. ScNaa15 has a high degree of structural conservation with SpNaa15 and hNaa15 structures, and ScNaa10 is similarly and completely locked into a cradle by the surrounding Naa15 helices. ScNaa50 has a robust interaction with ScNatA that is maintained even in high salt concentrations (1 M NaCl)
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additional information
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structure modeling and molecular docking of RimI, docking of the structure model of MtRimI-Ala-Arg-Tyr-Phe-Arg-Arg (ARYFRR) complex using the crystal structure of the RimI and bisubstrate from Salmonella typhimurium strain LT2 (PDB 2CNM) as template, overview. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
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additional information
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structure modeling and molecular docking of RimI, docking of the structure model of MtRimI-Ala-Arg-Tyr-Phe-Arg-Arg (ARYFRR) complex using the crystal structure of the RimI and bisubstrate from Salmonella typhimurium strain LT2 (PDB 2CNM) as template, overview. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
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F128I
site-directed mutagenesis, the mutation leads an altered structure and reduced stability, and a dramatic recuction of Nt catalytic activity compared to wild-type
F128L
site-directed mutagenesis, the mutation leads an altered structure and reduced stability, and a dramatic recuction of Nt catalytic activity compared to wild-type
I72T
a naturally occuring mutation NAA10 c.215T>C, the mutant phenotype shows a milder phenotypic spectrum in comparison to most of the previously described patients with NAA10 variants. The three boys have development delay, intellectual disability, and cardiac abnormalities as overlapping phenotypes. NAA10 Ile72Thr protein is destabilized, while binding to NAA15 most likely is intact. The NatA activity of NAA10 Ile72Thr appears normal while its monomeric activity is decreased. Genotype-phenotype correlations for NAA10 variants, overview
L814P
site-directed mutagenesis, the hNAA15 mutant is defective for HYPK inhibition and reduces hNatA thermostability, hNAA10 binding is not affected. The hNAA15-L814P-V5 hNatA complex shows an increased catalytic activity compared to wild-type hNatA
R116W
site-directed mutagenesis, the mutation leads to a reduction in catalytic activity for the peptide substrates EEEI and SESS by 15% compared to wild-type
R83C
site-directed mutagenesis, the mutation interferes with acetyl-CoA binding and leads to a 60% reduction in Nt-catalytic activity compared to wild-type
R83H
naturally occuring c.248G > A missense mutation, reduced enzymatic activity of monomeric NAA10-R83H. This variant is modelled to have an altered charge density in the acetyl-CoA binding region of NAA10
T406Y
site-directed mutagenesis, the hNAA15-T406Y-V5 hNatA mutant complex displays a decreased catalytic activity toward the hNatA substrate SESS compared to wild-type hNatA. the hNAA15 mutant can disassociate hNAA50 from hNatA in vitro, hNAA10 binding is not affected
V107F
site-directed mutagenesis, the mutation leads to a reduction in catalytic activity for the peptide substrates EEEI and SESS by 95% compared to wild-type
V111G
a naturally occuring 332 T > G missense mutant, the mutant Naa10 has a reduced stability and 85% reduced monomeric catalytic activity, while catalytic NatA function remains unaltered. NAA10-V111G has a reduced stability compared to wild-type NAA10, and in vitro acetylation assays reveal a reduced enzymatic activity of monomeric NAA10-V111G but not for NAA10-V111G in complex with NAA15 (NatA enzymatic activity). A glycine in position 111 instead of valine will not cause any steric clashes, but loss of the more bulky hydrophobic side chain of valine may possibly cause structural alterations affecting protein stability or acetyl-CoA binding
Y43S
site-directed mutagenesis, the mutant is catalytically impaired in vitro, with approximately an 85% reduction in Nt-catalytic activity for peptide substrates EEEI, DDDI, and SESS
N132A
the mutant shows 4.5fold increase in Km, with no significant difference in kcat compared to the wild type enzyme
R100A
the mutant shows 7fold increase in Km, with no significant difference in kcat compared to the wild type enzyme
T105A
the mutant shows 3fold increase in Km, with no significant difference in kcat compared to the wild type enzyme
E24A
mutation in NatA, decrease in kcat, increase in Km value
E24D
mutation in NatA, decrease in kcat, increase in Km value
E24Q
mutation in NatA, decrease in kcat, increase in Km value
E61A
mutation in NatA, decrease in kcat, increase in Km value
E62A
mutation in NatA, decrease in kcat, increase in Km value
H111A
mutation in NatA, decrease in kcat, Km value similar to wild-type
H20A
mutation in NatA, decrease in kcat, increase in Km value
H72A
mutation in NatA, decrease in kcat, increase in Km value
K29A
mutation in NatA, increase in kcat, decrease in Km value
K29A/Y33A
mutation in NatA, decrease in kcat, Km value similar to wild-type
K59A
mutation in NatA, decrease in kcat, increase in Km value
K59A/E61A
mutation in NatA, decrease in kcat, increase in Km value
K59A/E62A
mutation in NatA, decrease in kcat, increase in Km value
L22A
mutation in NatA, decrease in kcat, increase in Km value
P23A
mutation in NatA, decrease in kcat, increase in Km value
R113A
mutation in NatA, strong decrease in kcat, Km value similar to wild-type
R80A
mutation in NatA, decrease in kcat, increase in Km value
Y139A
mutation in NatA, dramaitc loss of activity
Y26A
mutation in NatA, decrease in kcat, increase in Km value
Y33A
mutation in NatA, decrease in kcat, increase in Km value
K136R
site-directed mutagenesis, that lacks autoacetylation, the mutant shows wild-type NAT activity
K136R
site-directed mutagenesis, the non-acetylated K136R mutant shows N-terminal acetyltransferase capacity as strongly as the hARD1/NAA10 wild-type, but fails to acetylate itself
R82A/Y122F
site-directed mutagenesis, the mutant shows highly reduced NAT activity compared to wild-type
R82A/Y122F
the acetyltransferase dead DN mutant of hARD1/NAA10 almost loses its NAT activity and fails to acetylate itself. The DN mutant includes two mutations R82A and Y122F, which inhibit the binding of acetyl-CoA to hARD1/NAA10 and consequently suppresses its acetyltransferase activity
S37P
the mutation is the cause of Ogden Syndrome
S37P
site-directed mutagenesis, the mutant Naa10 protein shows reduced catalytic activity for EEEI, DDDI, and SESS peptide substrates, and inability to combine with Naa15. The mutant hNaa10 S37P recombinantly expressed in a NatA-defective Saccharomyces cerevisiae strain lacks a proper complex formation with hNaa15 and is reduced in in vitro catalytic activity
S39P
site-directed mutagenesis, the mutation does not cause a phenotype
S39P
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site-directed mutagenesis, the mutation does not cause a phenotype
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additional information
generation of mutant naa10-1 and of a naa15 mutant by T-DNA insertion-disrupting gene expression
additional information
enzyme knockdown by siRNA. Generation of mutant daf-31(m655) by removal of 151 bp of promoter upstream of the ATG start codon and 242 bp of daf-31 coding region dowstream of the ATG start codon. Generation of and overexpression mutant daf-31 OE for which the full-length dar-31 genomic DNA is cloned into pGEM-T vector. Generation of mutant vncBDk by with impaired N-terminal activity
additional information
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enzyme knockdown by siRNA. Generation of mutant daf-31(m655) by removal of 151 bp of promoter upstream of the ATG start codon and 242 bp of daf-31 coding region dowstream of the ATG start codon. Generation of and overexpression mutant daf-31 OE for which the full-length dar-31 genomic DNA is cloned into pGEM-T vector. Generation of mutant vncBDk by with impaired N-terminal activity
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additional information
generation of mutant naa10MO by morpholino-based knockdown
additional information
generation of enzyme mutant by frame shift mutation causing a acetyltransferase-truncated enzymatic region, and of another mutant vnc by intron-insertion mutation
additional information
construction of Naa10 stably knocked down H1299 cell line H1299-shNaa10, cDNA microarray analysis
additional information
knockdown of Naa10p by shRNAs, knockdown efficiencies, overview. Generation of truncated Naa10p mutants
additional information
silencing of mouse immortalized embryonic endothelial cells
additional information
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silencing of mouse immortalized embryonic endothelial cells
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additional information
generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
additional information
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generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
additional information
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generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
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additional information
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generation of mutants MtRimI4-158, MtRimI1-153, MtRimI4-153, MtRimIC21A, and of the final construct MtRimIC21A4-153, MtRimIC21A4-153 has almost identical enzymatic activity compared to MtRimI, indicating insignificant influence of the recombinant variations on enzymatic functions. The 2D 1H-15N heteronuclear single quantum coherence spectrum of tRimIC21A4-153 exhibits wider chemical shift dispersion and favorable peak isolation, indicating that MtRimIC21A4-153 is amendable for further structural determination. Moreover, bio-layer interferometry experiments show that MtRimIC21A4-153 possesses similar micromolar affinity to full-length MtRimI for binding the hexapeptide substrate Ala-Arg-Tyr-Phe-Arg-Arg. Structure comparison of wild-type MtRimI and mutant MtRimIC21A4-153
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additional information
mutation ard1::HIS3 is caused by inserting a Barn HI fragment containinng the HIS3 gene into the Barn HI site of plasmid YCpE18 that lies within the functional sequence of ARD1. Genes nat1/ard1 double mutant nat1-5::LEU;ard1 is generated by mating of nat1 and ard1 single mutants, the single mutants of nat1 (Naa15) and ard1 (Naa10) display identical phenotypes, no additional phenotypes are found in the double mutant. Recombinant expression of the S37P mutant of human Naa10 in a NatA-defective yeast strain, the hNaa10 expressing mutant strain shows a lack of proper complex formation with hNaa15 and reduced in vitro catalytic activity, a decrease of Nt-acetylome and an increase in the Hsp70 family proteins
additional information
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mutation ard1::HIS3 is caused by inserting a Barn HI fragment containinng the HIS3 gene into the Barn HI site of plasmid YCpE18 that lies within the functional sequence of ARD1. Genes nat1/ard1 double mutant nat1-5::LEU;ard1 is generated by mating of nat1 and ard1 single mutants, the single mutants of nat1 (Naa15) and ard1 (Naa10) display identical phenotypes, no additional phenotypes are found in the double mutant. Recombinant expression of the S37P mutant of human Naa10 in a NatA-defective yeast strain, the hNaa10 expressing mutant strain shows a lack of proper complex formation with hNaa15 and reduced in vitro catalytic activity, a decrease of Nt-acetylome and an increase in the Hsp70 family proteins
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additional information
generation of an Ard1 null mutant by removal of the ARD1 coding region
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Polevoda, B.; Sherman, F.
Composition and function of the eukaryotic N-terminal acetyltransferase subunits
Biochem. Biophys. Res. Commun.
308
1-11
2003
Saccharomyces cerevisiae
brenda
Sugiura, N.; Adams, S.M.; Corriveau, R.A.
An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development
J. Biol. Chem.
278
40113-40120
2003
Mus musculus
brenda
Gautschi, M.; Just, S.; Mun, A.; Ross, S.; Rcknagel, P.; Dubaquie, Y.; Ehrenhofer-Murray, A.; Rospert, S.
The yeast Nalpha-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides
Mol. Cell. Biol.
23
7403-7414
2003
Saccharomyces cerevisiae, Saccharomyces cerevisiae MH272-3f a/alpha
brenda
Geissenhoener, A.; Weise, C.; Ehrenhofer-Murray, A.E.
Dependence of ORC silencing function on NatA-mediated Na acetylation in Saccharomyces cerevisiae
Mol. Cell. Biol.
24
10300-10312
2004
Saccharomyces cerevisiae
brenda
Arnesen, T.; Gromyko, D.; Kagabo, D.; Betts, M.; Starheim, K.; Varhaug, J.; Anderson, D.; Lillehaug, J.
A novel human NatA N-terminal acetyltransferase complex: HNaa16p-hNaa10p (hNat2-hArd1)
BMC Biochem.
10
15
2009
Homo sapiens
brenda
Ohkawa, N.; Sugisaki, S.; Tokunaga, E.; Fujitani, K.; Hayasaka, T.; Setou, M.; Inokuchi, K.
N-acetyltransferase ARD1-NAT1 regulates neuronal dendritic development
Genes Cells
13
1171-1183
2008
Mus musculus (Q9QY36)
brenda
Pezza, J.A.; Langseth, S.X.; Raupp Yamamoto, R.; Doris, S.M.; Ulin, S.P.; Salomon, A.R.; Serio, T.R.
The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype
Mol. Biol. Cell
20
1068-1080
2009
Saccharomyces cerevisiae
brenda
Perrot, M.; Massoni, A.; Boucherie, H.
Sequence requirements for Nalpha-terminal acetylation of yeast proteins by NatA
Yeast
25
513-527
2008
Saccharomyces cerevisiae
brenda
Wang, Y.; Mijares, M.; Gall, M.; Turan, T.; Javier, A.; Bornemann, D.; Manage, K.; Warrior, R.
Drosophila variable nurse cells encodes arrest defective 1 (ARD1), the catalytic subunit of the major N-terminal acetyltransferase complex
Dev. Dyn.
239
2813-2827
2010
Drosophila melanogaster (Q9VT75)
brenda
Arnesen, T.; Starheim, K.K.; Van Damme, P.; Evjenth, R.; Dinh, H.; Betts, M.J.; Ryningen, A.; Vandekerckhove, J.; Gevaert, K.; Anderson, D.
The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation
Mol. Cell. Biol.
30
1898-1909
2010
Homo sapiens
brenda
Chang, Y.Y.; Hsu, C.H.
Structural basis for substrate-specific acetylation of Nalpha-acetyltransferase Ard1 from Sulfolobus solfataricus
Sci. Rep.
5
8673
2015
Saccharolobus solfataricus (Q980R9)
brenda
Ree, R.; Myklebust, L.; Thiel, P.; Foyn, H.; Fladmark, K.; Arnesen, T.
The N-terminal acetyltransferase Naa10 is essential for zebrafish development
Biosci. Rep.
35
e00249
2015
Danio rerio (Q7T3B8), Danio rerio
brenda
Seo, J.H.; Park, J.H.; Lee, E.J.; Kim, K.W.
Different subcellular localizations and functions of human ARD1 variants
Int. J. Oncol.
46
701-707
2015
Homo sapiens (Q6P4J0)
brenda
Eiyama, A.; Okamoto, K.
Protein N-terminal acetylation by the NatA complex is critical for selective mitochondrial degradation
J. Biol. Chem.
290
25034-25044
2015
Saccharomyces cerevisiae
brenda
Magin, R.S.; March, Z.M.; Marmorstein, R.
The N-terminal acetyltransferase Naa10/ARD1 does not acetylate lysine residues
J. Biol. Chem.
291
5270-5277
2016
Homo sapiens
brenda
Liszczak, G.; Goldberg, J.M.; Foyn, H.; Petersson, E.J.; Arnesen, T.; Marmorstein, R.
Molecular basis for N-terminal acetylation by the heterodimeric NatA complex
Nat. Struct. Mol. Biol.
20
1098-1105
2013
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